ID   XYN1_HUMIN              Reviewed;         227 AA.
AC   P55334; Q12625;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-FEB-2023, entry version 90.
DE   RecName: Full=Endo-1,4-beta-xylanase 1;
DE            Short=Xylanase 1;
DE            EC=3.2.1.8;
DE   AltName: Full=1,4-beta-D-xylan xylanohydrolase 1;
DE   Flags: Precursor;
GN   Name=XYL1;
OS   Humicola insolens (Soft-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Humicola.
OX   NCBI_TaxID=34413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8190078; DOI=10.1007/bf00301060;
RA   Dalboege H., Hansen H.P.H.;
RT   "A novel method for efficient expression cloning of fungal enzyme genes.";
RL   Mol. Gen. Genet. 243:253-260(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8;
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000305}.
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DR   EMBL; X76047; CAA53632.1; -; mRNA.
DR   PIR; S43919; S43919.
DR   AlphaFoldDB; P55334; -.
DR   SMR; P55334; -.
DR   CAZy; GH11; Glycoside Hydrolase Family 11.
DR   CLAE; XYN11A_HUMIN; -.
DR   UniPathway; UPA00114; -.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..227
FT                   /note="Endo-1,4-beta-xylanase 1"
FT                   /id="PRO_0000008007"
FT   DOMAIN          37..225
FT                   /note="GH11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10062"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10063"
SQ   SEQUENCE   227 AA;  25601 MW;  5C2FF6ADCFEADA1F CRC64;
     MVSLKSVLAA ATAVSSAIAA PFDFVPRDNS TALQARQVTP NAEGWHNGYF YSWWSDGGGQ
     VQYTNLEGSR YQVRWRNTGN FVGGKGWNPG TGRTINYGGY FNPQGNGYLA VYGWTRNPLV
     EYYVIESYGT YNPGSQAQYK GTFYTDGDQY DIFVSTRYNQ PSIDGTRTFQ QYWSIRKNKR
     VGGSVNMQNH FNAWQQHGMP LGQHYYQVVA TEGYQSSGES DIYVQTH
//